Publication Date:
1990-05-18
Description:
Most proteins destined for export from Escherichia coli are made as precursors containing amino-terminal leader sequences that are essential for export and that are removed during the process. The initial step in export of a subset of proteins, which includes maltose-binding protein, is binding of the precursor by the molecular chaperone SecB. This work shows directly that SecB binds with high affinity to unfolded maltose-binding protein but does not specifically recognize and bind the leader. Rather, the leader modulates folding to expose elements in the remainder of the polypeptide that are recognized by SecB.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Randall, L L -- Topping, T B -- Hardy, S J -- GM 29798/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 May 18;248(4957):860-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biochemistry/Biophysics Program, Washington State University, Pullman 99164-4660.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2188362" target="_blank"〉PubMed〈/a〉
Keywords:
*ATP-Binding Cassette Transporters
;
Bacterial Proteins/*metabolism
;
Binding Sites
;
Biological Transport
;
Carrier Proteins/*metabolism
;
Cytosol/metabolism
;
Escherichia coli/*metabolism
;
*Escherichia coli Proteins
;
Maltose-Binding Proteins
;
Molecular Weight
;
*Monosaccharide Transport Proteins
;
Protein Conformation
;
Protein Precursors/*metabolism
;
Protein Sorting Signals/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
